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P04896

- GNAS2_BOVIN

UniProt

P04896 - GNAS2_BOVIN

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Protein

Guanine nucleotide-binding protein G(s) subunit alpha isoforms short

Gene

GNAS

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. The G(s) protein is involved in hormonal regulation of adenylate cyclase: it activates the cyclase in response to beta-adrenergic stimuli. Stimulates the Ras signaling pathway via RAPGEF2 By similarity.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi54 – 541MagnesiumBy similarity
Metal bindingi204 – 2041MagnesiumBy similarity
Binding sitei366 – 3661GTP; via amide nitrogenBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi47 – 548GTPBy similarity
Nucleotide bindingi198 – 2047GTPBy similarity
Nucleotide bindingi223 – 2275GTPBy similarity
Nucleotide bindingi292 – 2954GTPBy similarity

GO - Molecular functioni

  1. GTPase activity Source: InterPro
  2. GTP binding Source: UniProtKB-KW
  3. metal ion binding Source: UniProtKB-KW
  4. signal transducer activity Source: UniProtKB

GO - Biological processi

  1. adenylate cyclase-activating adrenergic receptor signaling pathway Source: UniProtKB
  2. adenylate cyclase-activating dopamine receptor signaling pathway Source: Ensembl
  3. cartilage development Source: Ensembl
  4. cognition Source: Ensembl
  5. developmental growth Source: Ensembl
  6. DNA methylation Source: Ensembl
  7. embryonic cranial skeleton morphogenesis Source: Ensembl
  8. embryonic hindlimb morphogenesis Source: Ensembl
  9. endochondral ossification Source: Ensembl
  10. energy reserve metabolic process Source: Ensembl
  11. genetic imprinting Source: Ensembl
  12. hair follicle placode formation Source: Ensembl
  13. multicellular organism growth Source: Ensembl
  14. platelet aggregation Source: Ensembl
  15. positive regulation of cAMP biosynthetic process Source: UniProtKB
  16. positive regulation of cAMP-mediated signaling Source: UniProtKB
  17. positive regulation of osteoblast differentiation Source: Ensembl
  18. positive regulation of osteoclast differentiation Source: Ensembl
  19. positive regulation of Ras GTPase activity Source: UniProtKB
  20. post-embryonic body morphogenesis Source: Ensembl
  21. response to drug Source: Ensembl
  22. tissue homeostasis Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Transducer

Keywords - Ligandi

GTP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_202137. Regulation of water balance by renal Aquaporins.
REACT_206547. G alpha (s) signalling events.
REACT_209033. G alpha (z) signalling events.
REACT_210568. G alpha (i) signalling events.
REACT_217846. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
REACT_219718. PKA activation in glucagon signalling.
REACT_220607. Glucagon-type ligand receptors.
REACT_221707. Glucagon signaling in metabolic regulation.
REACT_227415. Prostacyclin signalling through prostacyclin receptor.

Names & Taxonomyi

Protein namesi
Recommended name:
Guanine nucleotide-binding protein G(s) subunit alpha isoforms short
Alternative name(s):
Adenylate cyclase-stimulating G alpha protein
Gene namesi
Name:GNAS
Synonyms:GNAS1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Unplaced

Subcellular locationi

Cell membrane By similarity; Lipid-anchor By similarity

GO - Cellular componenti

  1. dendrite Source: Ensembl
  2. extracellular vesicular exosome Source: Ensembl
  3. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 394394Guanine nucleotide-binding protein G(s) subunit alpha isoforms shortPRO_0000203717Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-palmitoyl glycine1 Publication
Lipidationi3 – 31S-palmitoyl cysteine1 Publication
Cross-linki300 – 300Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei352 – 3521PhosphoserineBy similarity

Keywords - PTMi

Isopeptide bond, Lipoprotein, Palmitate, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiP04896.

Expressioni

Gene expression databases

ExpressionAtlasiP04896. baseline.

Interactioni

Subunit structurei

G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site. Interacts with CRY1; the interaction may block GPCR-mediated regulation of cAMP concentrations.

Protein-protein interaction databases

DIPiDIP-588N.
IntActiP04896. 1 interaction.
STRINGi9913.ENSBTAP00000023234.

Structurei

Secondary structure

1
394
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi36 – 394
Beta strandi40 – 489
Helixi53 – 6412
Helixi87 – 893
Helixi90 – 11223
Beta strandi113 – 1153
Helixi122 – 1243
Helixi125 – 1339
Turni134 – 1363
Helixi144 – 15512
Helixi157 – 1637
Helixi164 – 1685
Helixi175 – 1795
Helixi182 – 1854
Beta strandi187 – 1893
Helixi194 – 1996
Beta strandi206 – 2149
Beta strandi217 – 2248
Helixi228 – 23710
Turni238 – 2403
Beta strandi243 – 2497
Helixi252 – 2543
Turni258 – 2603
Beta strandi261 – 2644
Helixi265 – 27713
Helixi280 – 2823
Beta strandi283 – 2853
Beta strandi287 – 2926
Helixi294 – 30310
Helixi308 – 3103
Helixi313 – 3164
Helixi332 – 35019
Turni354 – 3563
Beta strandi359 – 3635
Beta strandi365 – 3673
Helixi369 – 39224

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AZSX-ray2.30C1-394[»]
1AZTX-ray2.30A/B1-394[»]
1CJKX-ray3.00C1-394[»]
1CJTX-ray2.80C1-394[»]
1CJUX-ray2.80C1-394[»]
1CJVX-ray3.00C1-394[»]
1CS4X-ray2.50C1-394[»]
1CULX-ray2.40C1-394[»]
1TL7X-ray2.80C1-394[»]
1U0HX-ray2.90C1-394[»]
2GVDX-ray2.90C1-394[»]
2GVZX-ray3.27C1-394[»]
3C14X-ray2.68C1-394[»]
3C15X-ray2.78C1-394[»]
3C16X-ray2.87C1-394[»]
3G82X-ray3.11C1-394[»]
3MAAX-ray3.00C1-394[»]
3SN6X-ray3.20A1-394[»]
ProteinModelPortaliP04896.
SMRiP04896. Positions 35-391.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04896.

Family & Domainsi

Sequence similaritiesi

Belongs to the G-alpha family. G(s) subfamily.Curated

Phylogenomic databases

eggNOGiNOG325092.
HOGENOMiHOG000038729.
HOVERGENiHBG063184.
InParanoidiP04896.
KOiK04632.

Family and domain databases

Gene3Di1.10.400.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR000367. Gprotein_alpha_S.
IPR001019. Gprotein_alpha_su.
IPR011025. GproteinA_insert.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR10218. PTHR10218. 1 hit.
PfamiPF00503. G-alpha. 1 hit.
[Graphical view]
PRINTSiPR00318. GPROTEINA.
PR00443. GPROTEINAS.
SMARTiSM00275. G_alpha. 1 hit.
[Graphical view]
SUPFAMiSSF47895. SSF47895. 1 hit.
SSF52540. SSF52540. 2 hits.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform Gnas-1 (identifier: P04896-1) [UniParc]FASTAAdd to Basket

Also known as: Alpha-S2

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGCLGNSKTE DQRNEEKAQR EANKKIEKQL QKDKQVYRAT HRLLLLGAGE
60 70 80 90 100
SGKSTIVKQM RILHVNGFNG EGGEEDPQAA RSNSDGEKAT KVQDIKNNLK
110 120 130 140 150
EAIETIVAAM SNLVPPVELA NPENQFRVDY ILSVMNVPDF DFPPEFYEHA
160 170 180 190 200
KALWEDEGVR ACYERSNEYQ LIDCAQYFLD KIDVIKQDDY VPSDQDLLRC
210 220 230 240 250
RVLTSGIFET KFQVDKVNFH MFDVGGQRDE RRKWIQCFND VTAIIFVVAS
260 270 280 290 300
SSYNMVIRED NQTNRLQEAL NLFKSIWNNR WLRTISVILF LNKQDLLAEK
310 320 330 340 350
VLAGKSKIED YFPEFARYTT PEDATPEPGE DPRVTRAKYF IRDEFLRIST
360 370 380 390
ASGDGRHYCY PHFTCAVDTE NIRRVFNDCR DIIQRMHLRQ YELL
Length:394
Mass (Da):45,709
Last modified:August 13, 1987 - v1
Checksum:i4D07A734AFF2A6BC
GO
Isoform Gnas-2 (identifier: P04896-2) [UniParc]FASTAAdd to Basket

Also known as: Alpha-S1

The sequence of this isoform differs from the canonical sequence as follows:
     71-84: Missing.

Show »
Length:380
Mass (Da):44,280
Checksum:i5B06C75B1A366920
GO
Isoform Nesp55 (identifier: O18979-1) [UniParc]FASTAAdd to Basket

The sequence of this isoform can be found in the external entry O18979.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

Note: Shares no sequence similarity with other isoforms due to a novel first exon containing the entire reading frame spliced to shared exon 2 so that exons 2-13 make up the 3'-UTR.

Length:241
Mass (Da):27,494
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti18 – 181A → G in AAA30560. (PubMed:3081893)Curated
Sequence conflicti85 – 851D → S in AAA30560. (PubMed:3081893)Curated
Sequence conflicti363 – 3631F → S in AAA30560. (PubMed:3081893)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei71 – 8414Missing in isoform Gnas-2. CuratedVSP_001832Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X03404 mRNA. Translation: CAA27137.1.
M13006 mRNA. Translation: AAA30560.1.
BC102905 mRNA. Translation: AAI02906.1.
BC122757 mRNA. Translation: AAI22758.1.
M14014 mRNA. Translation: AAA30557.1.
PIRiA23818. RGBOGA.
I45904.
RefSeqiNP_001258700.1. NM_001271771.1.
NP_851364.1. NM_181021.3. [P04896-1]
UniGeneiBt.64619.
Bt.91987.

Genome annotation databases

GeneIDi281793.
KEGGibta:281793.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X03404 mRNA. Translation: CAA27137.1 .
M13006 mRNA. Translation: AAA30560.1 .
BC102905 mRNA. Translation: AAI02906.1 .
BC122757 mRNA. Translation: AAI22758.1 .
M14014 mRNA. Translation: AAA30557.1 .
PIRi A23818. RGBOGA.
I45904.
RefSeqi NP_001258700.1. NM_001271771.1.
NP_851364.1. NM_181021.3. [P04896-1 ]
UniGenei Bt.64619.
Bt.91987.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AZS X-ray 2.30 C 1-394 [» ]
1AZT X-ray 2.30 A/B 1-394 [» ]
1CJK X-ray 3.00 C 1-394 [» ]
1CJT X-ray 2.80 C 1-394 [» ]
1CJU X-ray 2.80 C 1-394 [» ]
1CJV X-ray 3.00 C 1-394 [» ]
1CS4 X-ray 2.50 C 1-394 [» ]
1CUL X-ray 2.40 C 1-394 [» ]
1TL7 X-ray 2.80 C 1-394 [» ]
1U0H X-ray 2.90 C 1-394 [» ]
2GVD X-ray 2.90 C 1-394 [» ]
2GVZ X-ray 3.27 C 1-394 [» ]
3C14 X-ray 2.68 C 1-394 [» ]
3C15 X-ray 2.78 C 1-394 [» ]
3C16 X-ray 2.87 C 1-394 [» ]
3G82 X-ray 3.11 C 1-394 [» ]
3MAA X-ray 3.00 C 1-394 [» ]
3SN6 X-ray 3.20 A 1-394 [» ]
ProteinModelPortali P04896.
SMRi P04896. Positions 35-391.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-588N.
IntActi P04896. 1 interaction.
STRINGi 9913.ENSBTAP00000023234.

Proteomic databases

PRIDEi P04896.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 281793.
KEGGi bta:281793.

Organism-specific databases

CTDi 2778.

Phylogenomic databases

eggNOGi NOG325092.
HOGENOMi HOG000038729.
HOVERGENi HBG063184.
InParanoidi P04896.
KOi K04632.

Enzyme and pathway databases

Reactomei REACT_202137. Regulation of water balance by renal Aquaporins.
REACT_206547. G alpha (s) signalling events.
REACT_209033. G alpha (z) signalling events.
REACT_210568. G alpha (i) signalling events.
REACT_217846. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
REACT_219718. PKA activation in glucagon signalling.
REACT_220607. Glucagon-type ligand receptors.
REACT_221707. Glucagon signaling in metabolic regulation.
REACT_227415. Prostacyclin signalling through prostacyclin receptor.

Miscellaneous databases

EvolutionaryTracei P04896.
NextBioi 20805706.

Gene expression databases

ExpressionAtlasi P04896. baseline.

Family and domain databases

Gene3Di 1.10.400.10. 1 hit.
3.40.50.300. 2 hits.
InterProi IPR000367. Gprotein_alpha_S.
IPR001019. Gprotein_alpha_su.
IPR011025. GproteinA_insert.
IPR027417. P-loop_NTPase.
[Graphical view ]
PANTHERi PTHR10218. PTHR10218. 1 hit.
Pfami PF00503. G-alpha. 1 hit.
[Graphical view ]
PRINTSi PR00318. GPROTEINA.
PR00443. GPROTEINAS.
SMARTi SM00275. G_alpha. 1 hit.
[Graphical view ]
SUPFAMi SSF47895. SSF47895. 1 hit.
SSF52540. SSF52540. 2 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Primary structure of the alpha-subunit of bovine adenylate cyclase-stimulating G-protein deduced from the cDNA sequence."
    Nukada T., Tanabe T., Takahashi H., Noda M., Hirose T., Inayama S., Numa S.
    FEBS Lett. 195:220-224(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Deduced primary structure of the alpha subunit of the GTP-binding stimulatory protein of adenylate cyclase."
    Robishaw J.D., Russell D.W., Harris B.A., Smigel M.D., Gilman A.G.
    Proc. Natl. Acad. Sci. U.S.A. 83:1251-1255(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. NIH - Mammalian Gene Collection (MGC) project
    Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Hypothalamus and Kidney.
  4. "Molecular basis for two forms of the G protein that stimulates adenylate cyclase."
    Robishaw J.D., Smigel M.D., Gilman A.G.
    J. Biol. Chem. 261:9587-9590(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 69-90.
  5. "Galpha(s) is palmitoylated at the N-terminal glycine."
    Kleuss C., Krause E.
    EMBO J. 22:826-832(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PALMITOYLATION AT GLY-2 AND CYS-3, IDENTIFICATION BY MASS SPECTROMETRY.
  6. "Crystal structure of the adenylyl cyclase activator Gsalpha."
    Sunahara R.K., Tesmer J.J.G., Gilman A.G., Sprang S.R.
    Science 278:1943-1947(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-394 OF GNAS-2 FORM.
  7. "Crystal structure of the catalytic domains of adenylyl cyclase in a complex with Gsalpha.GTPgammaS."
    Tesmer J.J.G., Sunahara R.K., Gilman A.G., Sprang S.R.
    Science 278:1907-1916(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF COMPLEX WITH CATALYTIC DOMAINS OF ADENYLATE CYCLASE.
  8. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF COMPLEX WITH CATALYTIC DOMAINS OF ADENYLATE CYCLASE.

Entry informationi

Entry nameiGNAS2_BOVIN
AccessioniPrimary (citable) accession number: P04896
Secondary accession number(s): Q0II85, Q3SZE7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: October 29, 2014
This is version 152 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

The GNAS locus is imprinted in a complex manner, giving rise to distinct paternally, maternally and biallelically expressed proteins.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3